MOES_LYTVA
ID MOES_LYTVA Reviewed; 572 AA.
AC P52962;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 25-MAY-2022, entry version 86.
DE RecName: Full=Moesin;
OS Lytechinus variegatus (Green sea urchin) (Echinus variegatus).
OC Eukaryota; Metazoa; Echinodermata; Eleutherozoa; Echinozoa; Echinoidea;
OC Euechinoidea; Echinacea; Temnopleuroida; Toxopneustidae; Lytechinus.
OX NCBI_TaxID=7654;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=7738093; DOI=10.1242/jcs.108.1.161;
RA Bachman E.S., McClay D.R.;
RT "Characterization of moesin in the sea urchin Lytechinus variegatus:
RT redistribution to the plasma membrane following fertilization is inhibited
RT by cytochalasin B.";
RL J. Cell Sci. 108:161-171(1995).
CC -!- FUNCTION: Probably involved in connections of major cytoskeletal
CC structures to the plasma membrane.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000250}; Peripheral membrane
CC protein {ECO:0000250}; Cytoplasmic side {ECO:0000250}. Cytoplasm,
CC cytoskeleton {ECO:0000250}. Cell projection {ECO:0000250}.
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DR EMBL; U14180; AAC46514.1; -; Genomic_DNA.
DR AlphaFoldDB; P52962; -.
DR SMR; P52962; -.
DR PRIDE; P52962; -.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-SubCell.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0003779; F:actin binding; IEA:InterPro.
DR CDD; cd14473; FERM_B-lobe; 1.
DR CDD; cd13194; FERM_C_ERM; 1.
DR Gene3D; 1.20.80.10; -; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 6.10.360.10; -; 1.
DR InterPro; IPR019749; Band_41_domain.
DR InterPro; IPR011174; ERM.
DR InterPro; IPR041789; ERM_FERM_C.
DR InterPro; IPR000798; Ez/rad/moesin-like.
DR InterPro; IPR014352; FERM/acyl-CoA-bd_prot_sf.
DR InterPro; IPR035963; FERM_2.
DR InterPro; IPR019748; FERM_central.
DR InterPro; IPR019747; FERM_CS.
DR InterPro; IPR000299; FERM_domain.
DR InterPro; IPR018979; FERM_N.
DR InterPro; IPR018980; FERM_PH-like_C.
DR InterPro; IPR008954; Moesin_tail_sf.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR PANTHER; PTHR23281; PTHR23281; 1.
DR Pfam; PF09380; FERM_C; 1.
DR Pfam; PF00373; FERM_M; 1.
DR Pfam; PF09379; FERM_N; 1.
DR PIRSF; PIRSF002305; ERM; 1.
DR PRINTS; PR00935; BAND41.
DR PRINTS; PR00661; ERMFAMILY.
DR SMART; SM00295; B41; 1.
DR SMART; SM01196; FERM_C; 1.
DR SUPFAM; SSF47031; SSF47031; 1.
DR SUPFAM; SSF48678; SSF48678; 1.
DR SUPFAM; SSF54236; SSF54236; 1.
DR PROSITE; PS00660; FERM_1; 1.
DR PROSITE; PS00661; FERM_2; 1.
DR PROSITE; PS50057; FERM_3; 1.
PE 3: Inferred from homology;
KW Cell membrane; Cell projection; Cytoplasm; Cytoskeleton; Membrane.
FT CHAIN 1..572
FT /note="Moesin"
FT /id="PRO_0000219420"
FT DOMAIN 1..294
FT /note="FERM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00084"
FT REGION 444..508
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 523..544
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..502
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 572 AA; 67579 MW; E1BA3F8E84B5E764 CRC64;
MPRGVAVRVT TMDAELEFAI QPNTTGKQLF DQVVKTIGLR EIWFFGLQYI DSKGLVTWLK
LNKKVVAQDL RKDNPLQFKF RVKFYPEEVT EELIQEITQR LFFLQIKEGI LSDEVYCPPE
TSVLLASYAA QAKYGPHSAS TKARLTEDTN ILPKRVIEQH KMTKEQWYER VSNWHQEHLS
LSKEDAITEY MKIAQDLEMY GVNYFEIRNK KGTDLWLGVD ALGLNVYEKD DKLTPKIGFP
WSEIRNISFN DKKFVIKPIE KKAPDFVFYA SRLRINKRIL ALCMGNHELY MRRRKPDTIE
VQQMKAQAKE EKQAKKLERE QLAIEMKKRQ ETEEKYKRLQ QQIREKELAE EKNREDLKRW
EEESRAMQEK LKQQQMESEE YQSKVAAMEM QMNEATLERE MTAQEKEEMR ARVEALAEEK
ARLEQSREES LKESAEFAEK LRLSQERERE LQEAQEAAAA QHAAQLAAQR EAQQLIPKDE
GEEDEQDHEL EVQQDDNDDL DDKESYLPDK HLLDKLQKLQ SELQAMKDES KGEDRYDKIH
QENIRAGRDK YQTLRNIRSG NTRQRIDTFE NI